ID A0A0V0XUJ0_TRIPS Unreviewed; 1797 AA.
AC A0A0V0XUJ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cytochrome b-c1 complex subunit 8 {ECO:0000256|ARBA:ARBA00016324, ECO:0000256|RuleBase:RU368118};
DE AltName: Full=Complex III subunit 8 {ECO:0000256|RuleBase:RU368118};
GN Name=Aats-ala {ECO:0000313|EMBL:KRX91579.1};
GN ORFNames=T4E_746 {ECO:0000313|EMBL:KRX91579.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX91579.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX91579.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX91579.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC complex plays an important role in the uptake of multiple carbon
CC sources present in different host niches.
CC {ECO:0000256|RuleBase:RU368118}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1. The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)). Interacts with
CC UQCC6. {ECO:0000256|RuleBase:RU368118}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU368118}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU368118}.
CC -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family.
CC {ECO:0000256|ARBA:ARBA00007668, ECO:0000256|RuleBase:RU368118}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX91579.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDU01000134; KRX91579.1; -; Genomic_DNA.
DR STRING; 6337.A0A0V0XUJ0; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:UniProtKB-UniRule.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:UniProtKB-UniRule.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 1.20.5.210; Cytochrome b-c1 complex subunit 8; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR004205; Cyt_bc1_su8.
DR InterPro; IPR036642; Cyt_bc1_su8_sf.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF39; ALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF02939; UcrQ; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR SUPFAM; SSF81508; Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU368118};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRX91579.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368118};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU368118};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU368118};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368118};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 996..1710
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 464..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1797 AA; 202098 MW; 4B4BD42CFF424D55 CRC64;
MSSVSLFLLN HRRKTASTYR RTCATAVGTD DQTPCQDSPP MEDVRANSNL ILADMIRELA
ALWNHADQLV NDFYLQLKHL DQRTDQAKSR LAHLNRRCRT LQLPPTDAAS AGSLRRFLSV
RNHYQSMKLE DDSNDGETIK TNYTNLFLPS TRPCYLIKFQ QELKKDEIAW SCMYTKKPTQ
TACIQTDPDE TFSNDVGFSV DFCRPRDRRK SSFSADPPLP TPEQQAQQLV ALCKPITLEI
NANGRACPAG NNVNNNQHKV SVFSEKSTFG RASQATGLSR LRLRSADGFS INIQSNDNDD
TYTGAVQQTV DLFECSAAKE YLYDFAPFYR RRTERLGGMK QFLSLRRPKK IHALHSTEKS
ANNSTDEYKS KPSDRIKTHF DIASISKFFK RSFSFRNTSS KPAVCVDKPI AACQSKTIAN
GTENSLETIE ESQESSRQIW LGKPKTSLPI STSSQVMNLA TLLRRSSRKV KPQESAERNQ
TAPSSRSSKD SAYMSGGERK ARVVSFLSAE SNTSLEVSDK KHASTYRVGF KLNYPEECKL
NIISNNNSLI SNSNIQTQHL IDLQRSEHTS QWVPGSPSVN SNCSAIDSNY SCDHEGYFTS
MHHDSGLPLP SYNCETVTDA GRGRSFSTHS SASTLADGAH LSQSESSSAT TPPASSFFPR
VSIHSSPCMQ TRTTAPQYIP HSIYVNSCPK VLSTEHQPFC SENPYVFGPH ATMNFNNLHS
QMQPNRVVPF MQCSGCRPLN SLSPARYVHL PSPLEANRIP EPTNFYYVQR NHCPLKVANG
YQQFNDAASL QSAVKNGEAW GMPCSQVFSC AQAQDNYGMY RPVESRTESS ATCCSNSQIP
EDDKMDPFDR WLVAKFCVEQ QEAKLKEAKL AERAKLAAWT CQKAKKTNEM RPWGRMAKIY
GMYQFSLSPF EQKAFGGYGK EIRNLGSKAF EYWWALLAIP ALYYLRDYGM KQEEKRLRKN
PADFICEIMR QVFLSSCNLT LHVVVRRLCT NANVKWNSRK VRQTFINYFK KWNHVVVESS
SVIAPKQSGM LFTSAGVVQF KPIISNLNVP VQQSRPMDSL GLAVSCQKCA RVNDLNLVGK
DRTHHTFFEM LGNWSFNGTM SKQTVCTHAW QLLTKIYCID EQRLHVTYFG GDKQLGLDAD
QECKQIWLDV VGVQQCRLLV GNAKENFWSI GETGPCGPCT EIHVQLPDGT LSELWNVVFM
EYYKHEDGSL QKLSATHVDT GMGLERLCAI LQNEDSAYGT DLFKPLIDSC QKLTGSPPYE
GRFGVDDVTG LDSSHRIIVD HARMCTFAIA DGLKPGHQEA GHVLRKIIRR ALYHVSLLGE
PRSGVFPNLC SAVVDLYADT YPQLQSSRRL VDQVLVEEEK RFSGTLTKAK ARFDRMQEPI
DPEVMFLFYN TYGLPMEMVQ NLAERRGVPF DLQEFEQCLQ EQRRRSLTNK QKQQLRVALQ
QLELPSNTDD TLKHSTMETQ TEDGSVAYQT ACCEGRVLAI LRSQTPVTEV TSDDQVQCSV
ILDKTSFYAT DDGQTGDRGI LRWREGEFLV DSTTSLEHVV LHHGRVLCGK LIAGQTSVHC
LVDVNSRTAC MQQHTALHLI LGILRQHLNI STEQPLTGMI NRQSAWIQFY SLQSVQSKNY
LLQLIDKHAN MLIEQNCPVI TQIMNLENAK LLLKDDFPRV IDSKTKTIRL VTLDIKPHPI
HQLCRAGMHV STLGKLYHIS PISLAEVNEG YSSLTLQDSA KIGLLFIMTL FGKCNATSGN
ALSITARNVP WQLRSLFVAS AQGRMQIFDV ACVSKFPCLR VGPLQYYSRN ADGLAQE
//
